ID S6D0R9_ACEPA Unreviewed; 643 AA.
AC S6D0R9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Ribonucleoside-diphosphate reductase {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
DE EC=1.17.4.1 {ECO:0000256|ARBA:ARBA00012274, ECO:0000256|RuleBase:RU003410};
GN Name=nrdA {ECO:0000313|EMBL:CCT60612.1};
GN ORFNames=APA386B_2577 {ECO:0000313|EMBL:CCT60612.1};
OS Acetobacter pasteurianus 386B.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=1266844 {ECO:0000313|EMBL:CCT60612.1, ECO:0000313|Proteomes:UP000015386};
RN [1] {ECO:0000313|EMBL:CCT60612.1, ECO:0000313|Proteomes:UP000015386}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=386B {ECO:0000313|EMBL:CCT60612.1};
RX PubMed=23902333;
RA Illeghems K., De Vuyst L., Weckx S.;
RT "Complete genome sequence and comparative analysis of Acetobacter
RT pasteurianus 386B, a strain well-adapted to the cocoa bean fermentation
RT ecosystem.";
RL BMC Genomics 14:526-526(2013).
CC -!- FUNCTION: Provides the precursors necessary for DNA synthesis.
CC Catalyzes the biosynthesis of deoxyribonucleotides from the
CC corresponding ribonucleotides. {ECO:0000256|RuleBase:RU003410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-
CC diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-
CC diphosphate; Xref=Rhea:RHEA:23252, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC COMP:10700, ChEBI:CHEBI:15377, ChEBI:CHEBI:29950, ChEBI:CHEBI:50058,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:73316; EC=1.17.4.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000206,
CC ECO:0000256|RuleBase:RU003410};
CC -!- SIMILARITY: Belongs to the ribonucleoside diphosphate reductase large
CC chain family. {ECO:0000256|ARBA:ARBA00010406,
CC ECO:0000256|RuleBase:RU003410}.
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DR EMBL; HF677570; CCT60612.1; -; Genomic_DNA.
DR RefSeq; WP_003622955.1; NC_021991.1.
DR AlphaFoldDB; S6D0R9; -.
DR GeneID; 66350177; -.
DR KEGG; apk:APA386B_2577; -.
DR PATRIC; fig|1266844.4.peg.2569; -.
DR HOGENOM; CLU_000404_7_0_5; -.
DR UniPathway; UPA00326; -.
DR Proteomes; UP000015386; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004748; F:ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor; IEA:UniProtKB-EC.
DR GO; GO:0009263; P:deoxyribonucleotide biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR CDD; cd01679; RNR_I; 1.
DR Gene3D; 3.20.70.20; -; 1.
DR InterPro; IPR000788; RNR_lg_C.
DR InterPro; IPR013509; RNR_lsu_N.
DR InterPro; IPR008926; RNR_R1-su_N.
DR InterPro; IPR039718; Rrm1.
DR PANTHER; PTHR11573; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE CHAIN; 1.
DR PANTHER; PTHR11573:SF6; RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE LARGE SUBUNIT; 1.
DR Pfam; PF02867; Ribonuc_red_lgC; 2.
DR Pfam; PF00317; Ribonuc_red_lgN; 1.
DR PRINTS; PR01183; RIBORDTASEM1.
DR SUPFAM; SSF51998; PFL-like glycyl radical enzymes; 1.
DR SUPFAM; SSF48168; R1 subunit of ribonucleotide reductase, N-terminal domain; 1.
PE 3: Inferred from homology;
KW Deoxyribonucleotide synthesis {ECO:0000256|ARBA:ARBA00023116,
KW ECO:0000256|RuleBase:RU003410};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003410}.
FT DOMAIN 53..118
FT /note="Ribonucleotide reductase large subunit N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00317"
FT DOMAIN 122..442
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT DOMAIN 445..596
FT /note="Ribonucleotide reductase large subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02867"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 71699 MW; 746607CA7FCFD3E4 CRC64;
MTLIDVQEND IRRSSSGGAE AGEPDLFNAG KMEDMVQLPG HHQVRVDRSR DALLTPFGKA
TLDNRYLLPD EGYQDLFGRV ASYYGADAAH AQRIYDYISK HWFMPATPVL SNGGTSRGLP
ISCFLNEASD SLKGIVDLWN ENVWLASKGG GIGSYWGNLR SIGENVGRNG KTSGVIPFIR
VMDSLTLAIS QGSLRRGSAA VYLPVWHPEI EEFIELRRPT GGDPNRKALN LHHGVLVSDA
FMRAVESDDE WALISPKDGS VIRKISARGL WIRILTARME QGEPYIVYSD HVNNARPEHH
KLAGLEVKTS NLCSEITLPT GIDHHGKART AVCCLSSLNL ETWDQWKDNP QFIEDVMLFL
DNVLQDFIDR APEDMHRAKY AAMRERSVGL GVMGFHSFLQ SRNVPFESVV AKVWNRKIFK
HIREQADAAS RKLAELRGPC PDAEEYGIME RFSNKMAIAP TASISIIAGN ASPGIEPIAA
NVFLQKTLSG SFTVRNRHLQ KLLEEKGQDT PEVWSSITTS KGSVQHLDFL TQQEKDVFKT
AFELDQRWVV EHAADRQPFI CQAQSVNLFL PADVHKRDLH QIHYMAWKKG LKSLYYCRSL
SIQRADTVSN VLAKNDVMNV DSSQASSGSA SSGNDYEECL ACQ
//
